Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O54890 (ITB3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin beta-3
Alternative name(s):
Platelet membrane glycoprotein IIIa
Short name=GPIIIa
CD_antigen=CD61
Gene names
Name:Itgb3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length787 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Integrin alpha-V/beta-3 is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIB/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIB/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIB/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIB/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface.

Subunit structure

Heterodimer of an alpha and a beta subunit. Beta-3 associates with either alpha-IIB or alpha-V. Interacts with FLNB and COMP. Interacts with PDIA6 following platelet stimulation. Interacts with SYK; upon activation by ITGB3 promotes platelet adhesion. Interacts with MYO10 By similarity. Interacts with DAB2. Interacts with FERMT2. Ref.6 Ref.7

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

Phosphorylated on tyrosine residues in response to thrombin-induced platelet aggregation. Probably involved in outside-in signaling By similarity.

Sequence similarities

Belongs to the integrin beta chain family.

Contains 1 VWFA domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionIntegrin
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis involved in wound healing

Inferred from electronic annotation. Source: InterPro

cell projection morphogenesis

Inferred by curator PubMed 16995821. Source: BHF-UCL

cell-matrix adhesion

Inferred from genetic interaction PubMed 17099249. Source: MGI

cell-substrate junction assembly

Inferred from direct assay PubMed 12867986. Source: MGI

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

platelet aggregation

Inferred from electronic annotation. Source: InterPro

positive regulation of bone resorption

Inferred by curator PubMed 16995821. Source: BHF-UCL

positive regulation of cell migration

Inferred from mutant phenotype PubMed 20675382. Source: BHF-UCL

positive regulation of osteoblast proliferation

Inferred from mutant phenotype PubMed 20675382. Source: BHF-UCL

positive regulation of osteoclast differentiation

Inferred by curator PubMed 16995821. Source: BHF-UCL

regulation of cell migration

Inferred from mutant phenotype PubMed 15031111. Source: MGI

   Cellular_componentalpha9-beta1 integrin complex

Traceable author statement PubMed 16995821. Source: BHF-UCL

alpha9-beta1 integrin-ADAM8 complex

Inferred from direct assay PubMed 16995821. Source: BHF-UCL

apical plasma membrane

Inferred from direct assay PubMed 16216233. Source: MGI

external side of plasma membrane

Inferred from direct assay PubMed 12900455PubMed 9553049. Source: MGI

nucleus

Inferred from sequence orthology PubMed 22027834. Source: MGI

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

   Molecular_functionintegrin binding

Inferred from physical interaction PubMed 8601592. Source: MGI

receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 787762Integrin beta-3
PRO_0000016345

Regions

Topological domain26 – 717692Extracellular Potential
Transmembrane718 – 74023Helical; Potential
Topological domain741 – 78747Cytoplasmic Potential
Domain134 – 376243VWFA
Repeat462 – 51049I
Repeat511 – 55242II
Repeat553 – 59139III
Repeat592 – 62837IV
Region462 – 628167Cysteine-rich tandem repeats

Amino acid modifications

Modified residue7721Phosphotyrosine By similarity
Modified residue7781Phosphothreonine By similarity
Modified residue7841Phosphotyrosine By similarity
Glycosylation3451N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation4771N-linked (GlcNAc...) Potential
Glycosylation5841N-linked (GlcNAc...) Potential
Glycosylation6791N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 460 By similarity
Disulfide bond38 ↔ 48 By similarity
Disulfide bond41 ↔ 74 By similarity
Disulfide bond51 ↔ 63 By similarity
Disulfide bond202 ↔ 209 By similarity
Disulfide bond257 ↔ 298 By similarity
Disulfide bond399 ↔ 411 By similarity
Disulfide bond431 ↔ 680 By similarity
Disulfide bond458 ↔ 462 By similarity
Disulfide bond473 ↔ 485 By similarity
Disulfide bond482 ↔ 520 By similarity
Disulfide bond487 ↔ 496 By similarity
Disulfide bond498 ↔ 511 By similarity
Disulfide bond526 ↔ 531 By similarity
Disulfide bond528 ↔ 561 By similarity
Disulfide bond533 ↔ 546 By similarity
Disulfide bond548 ↔ 553 By similarity
Disulfide bond567 ↔ 572 By similarity
Disulfide bond569 ↔ 600 By similarity
Disulfide bond574 ↔ 583 By similarity
Disulfide bond585 ↔ 592 By similarity
Disulfide bond606 ↔ 611 By similarity
Disulfide bond608 ↔ 656 By similarity
Disulfide bond613 ↔ 623 By similarity
Disulfide bond626 ↔ 629 By similarity
Disulfide bond633 ↔ 642 By similarity
Disulfide bond639 ↔ 712 By similarity
Disulfide bond660 ↔ 688 By similarity

Experimental info

Sequence conflict1141A → V in AAB94086. Ref.1
Sequence conflict3891E → G in AAB94086. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O54890 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 4F2E606969788794

FASTA78786,738
        10         20         30         40         50         60 
MRAQWPGQLW AALLALGALA GVVVGESNIC TTRGVNSCQQ CLAVSPVCAW CSDETLSQGS 

        70         80         90        100        110        120 
PRCNLKENLL KDNCAPESIE FPVSEAQILE ARPLSSKGSG SSAQITQVSP QRIALRLRPD 

       130        140        150        160        170        180 
DSKIFSLQVR QVEDYPVDIY YLMDLSFSMK DDLSSIQTLG TKLASQMRKL TSNLRIGFGA 

       190        200        210        220        230        240 
FVDKPVSPYM YISPPQAIKN PCYNMKNACL PMFGYKHVLT LTDQVSRFNE EVKKQSVSRN 

       250        260        270        280        290        300 
RDAPEGGFDA IMQATVCDEK IGWRNDASHL LVFTTDAKTH IALDGRLAGI VLPNDGHCHI 

       310        320        330        340        350        360 
GTDNHYSAST TMDYPSLGLM TEKLSQKNIN LIFAVTENVV SLYQNYSELI PGTTVGVLSD 

       370        380        390        400        410        420 
DSSNVLQLIV DAYGKIRSKV ELEVRDLPEE LSLSFNATCL NNEVIPGLKS CVGLKIGDTV 

       430        440        450        460        470        480 
SFSIEAKVRG CPQEKEQSFT IKPVGFKDSL TVQVTFDCDC ACQAFAQPSS PRCNNGNGTF 

       490        500        510        520        530        540 
ECGVCRCDQG WLGSMCECSE EDYRPSQQEE CSPKEGQPIC SQRGECLCGQ CVCHSSDFGK 

       550        560        570        580        590        600 
ITGKYCECDD FSCVRYKGEM CSGHGQCNCG DCVCDSDWTG YYCNCTTRTD TCMSTNGLLC 

       610        620        630        640        650        660 
SGRGNCECGS CVCVQPGSYG DTCEKCPTCP DACSFKKECV ECKKFNRGTL HEENTCSRYC 

       670        680        690        700        710        720 
RDDIEQVKEL TDTGKNAVNC TYKNEDDCVV RFQYYEDTSG RAVLYVVEEP ECPKGPDILV 

       730        740        750        760        770        780 
VLLSVMGAIL LIGLATLLIW KLLITIHDRK EFAKFEEERA RAKWDTANNP LYKEATSTFT 


NITYRGT 

« Hide

References

« Hide 'large scale' references
[1]McHugh K.P., Teitelbaum S.L., Kitazawa S., Ross F.P.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H/HeN.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Inner ear.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"Integrin beta cytoplasmic domain interactions with phosphotyrosine-binding domains: a structural prototype for diversity in integrin signaling."
Calderwood D.A., Fujioka Y., de Pereda J.M., Garcia-Alvarez B., Nakamoto T., Margolis B., McGlade C.J., Liddington R.C., Ginsberg M.H.
Proc. Natl. Acad. Sci. U.S.A. 100:2272-2277(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2.
[7]"Kindlin-2 controls bidirectional signaling of integrins."
Montanez E., Ussar S., Schifferer M., Bosl M., Zent R., Moser M., Fassler R.
Genes Dev. 22:1325-1330(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FERMT2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF026509 mRNA. Translation: AAB94086.1.
AK157958 mRNA. Translation: BAE34283.1.
AL603709, BX000996 Genomic DNA. Translation: CAM22629.1.
BX000996, AL603709 Genomic DNA. Translation: CAM27926.1.
CH466558 Genomic DNA. Translation: EDL34227.1.
BC125518 mRNA. Translation: AAI25519.1.
BC125520 mRNA. Translation: AAI25521.1.
PIRPN0510.
RefSeqNP_058060.2. NM_016780.2.
UniGeneMm.87150.

3D structure databases

ProteinModelPortalO54890.
SMRO54890. Positions 28-787.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200830. 2 interactions.
DIPDIP-46416N.
IntActO54890. 4 interactions.
MINTMINT-4099028.
STRING10090.ENSMUSP00000021028.

Chemistry

BindingDBO54890.

PTM databases

PhosphoSiteO54890.

Proteomic databases

PaxDbO54890.
PRIDEO54890.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021028; ENSMUSP00000021028; ENSMUSG00000020689.
GeneID16416.
KEGGmmu:16416.
UCSCuc007lwx.2. mouse.

Organism-specific databases

CTD3690.
MGIMGI:96612. Itgb3.

Phylogenomic databases

eggNOGNOG287997.
GeneTreeENSGT00720000108389.
HOGENOMHOG000252936.
HOVERGENHBG006190.
InParanoidQ3TZC6.
KOK06493.
OMAGHGQCSC.
OrthoDBEOG7T7GSB.
TreeFamTF105392.

Gene expression databases

BgeeO54890.
CleanExMM_ITGB3.
GenevestigatorO54890.

Family and domain databases

Gene3D1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProIPR027068. Integrin_beta-3.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view]
PANTHERPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF25. PTHR10082:SF25. 1 hit.
PfamPF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFPIRSF002512. Integrin_B. 1 hit.
PRINTSPR01186. INTEGRINB.
SMARTSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITGB3. mouse.
NextBio289613.
PROO54890.
SOURCESearch...

Entry information

Entry nameITB3_MOUSE
AccessionPrimary (citable) accession number: O54890
Secondary accession number(s): Q3TZC6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot